TY - JOUR
T1 - Purification, crystallization and preliminary crystallographic characterization of the α2,6-sialyltransferase from Photobacterium sp. JT-ISH-224
AU - Okino, Nozomu
AU - Kakuta, Yoshimitsu
AU - Kajiwara, Hitomi
AU - Ichikawa, Masako
AU - Takakura, Yoshimitsu
AU - Ito, Makoto
AU - Yamamoto, Takeshi
PY - 2007/7/28
Y1 - 2007/7/28
N2 - Sialyltransferases transfer sialic acid from cytidine-5-monophospho-N- acetylneuraminic acid (CMP-NeuAc) to the nonreducing termini of the oligosaccharyl structures of various glycoproteins and glycolipids. The newly cloned α2,6-sialyltransferase from Photobacterium sp. JT-ISH-224 (from the Vibrionaceae family) is composed of two domains: an unknown N-terminal domain and a catalytic C-terminal domain which shares significant homology with the Pasteurella multocida multifunctional sialyltransferase. The putative mature form of JT-ISH-224 α2,6-sialyltransferase was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystal belonged to space group P3121 or P3 221, with unit-cell parameters a = b = 90.29, c = 204.33 Å. X-ray diffraction data were collected to 2.5 Å resolution.
AB - Sialyltransferases transfer sialic acid from cytidine-5-monophospho-N- acetylneuraminic acid (CMP-NeuAc) to the nonreducing termini of the oligosaccharyl structures of various glycoproteins and glycolipids. The newly cloned α2,6-sialyltransferase from Photobacterium sp. JT-ISH-224 (from the Vibrionaceae family) is composed of two domains: an unknown N-terminal domain and a catalytic C-terminal domain which shares significant homology with the Pasteurella multocida multifunctional sialyltransferase. The putative mature form of JT-ISH-224 α2,6-sialyltransferase was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystal belonged to space group P3121 or P3 221, with unit-cell parameters a = b = 90.29, c = 204.33 Å. X-ray diffraction data were collected to 2.5 Å resolution.
UR - http://www.scopus.com/inward/record.url?scp=34547631024&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34547631024&partnerID=8YFLogxK
U2 - 10.1107/S1744309107031363
DO - 10.1107/S1744309107031363
M3 - Article
C2 - 17671362
AN - SCOPUS:34547631024
SN - 1744-3091
VL - 63
SP - 662
EP - 664
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
IS - 8
ER -